data_4874 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific assignment of the PAH2 domain of Sin3B free and complexed to Mad1 ; _BMRB_accession_number 4874 _BMRB_flat_file_name bmr4874.str _Entry_type original _Submission_date 2000-10-23 _Accession_date 2000-10-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Spronk Christian A.E.M. . 2 Jansen Jacobus F.A. . 3 Tessari Marco . . 4 Kaan Anita M. . 5 Aelen Jan . . 6 Vermeulen Michiel . . 7 Stunnenberg Hendrik G. . 8 Vuister Geerten W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 102 "13C chemical shifts" 296 "15N chemical shifts" 102 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-04-26 original author . stop_ _Original_release_date 2001-04-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the editor: Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Spronk Christian A.E.M. . 2 Jansen Jacobus F.A. . 3 Tessari Marco . . 4 Kaan Anita M. . 5 Aelen Jan . . 6 Lasonder Edwin . . 7 Stunnenberg Hendrik G. . 8 Vuister Geerten W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 377 _Page_last 378 _Year 2001 _Details . loop_ _Keyword Sin3 Mad1 'transcriptional regulator' 'protein-peptide complex' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995) ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_citation_2 _Saveframe_category citation _Citation_full 'Ch. Bartels, et al. J. Biomol. NMR 6, 1-10 (1995).' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_mSin3B-PAH2 _Saveframe_category molecular_system _Mol_system_name 'mSin3B-PAH2 free state' _Abbreviation_common mSin3B-PAH2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PAH2 $mSin3B-PAH2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'transcriptional regulator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mSin3B-PAH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'mSin3B-PAH2 domain' _Abbreviation_common mSin3B-PAH2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; ESDSVEFNNAISYVNKIKTR FLDHPEIYRSFLEILHTYQK EQLHTKGRPFRGMSEEEVFT EVANLFRGQEDLLSEFGQFL PEAKRSLFTGNGSAEMNSGQ KNEEK ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 SER 3 ASP 4 SER 5 VAL 6 GLU 7 PHE 8 ASN 9 ASN 10 ALA 11 ILE 12 SER 13 TYR 14 VAL 15 ASN 16 LYS 17 ILE 18 LYS 19 THR 20 ARG 21 PHE 22 LEU 23 ASP 24 HIS 25 PRO 26 GLU 27 ILE 28 TYR 29 ARG 30 SER 31 PHE 32 LEU 33 GLU 34 ILE 35 LEU 36 HIS 37 THR 38 TYR 39 GLN 40 LYS 41 GLU 42 GLN 43 LEU 44 HIS 45 THR 46 LYS 47 GLY 48 ARG 49 PRO 50 PHE 51 ARG 52 GLY 53 MET 54 SER 55 GLU 56 GLU 57 GLU 58 VAL 59 PHE 60 THR 61 GLU 62 VAL 63 ALA 64 ASN 65 LEU 66 PHE 67 ARG 68 GLY 69 GLN 70 GLU 71 ASP 72 LEU 73 LEU 74 SER 75 GLU 76 PHE 77 GLY 78 GLN 79 PHE 80 LEU 81 PRO 82 GLU 83 ALA 84 LYS 85 ARG 86 SER 87 LEU 88 PHE 89 THR 90 GLY 91 ASN 92 GLY 93 SER 94 ALA 95 GLU 96 MET 97 ASN 98 SER 99 GLY 100 GLN 101 LYS 102 ASN 103 GLU 104 GLU 105 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 5457 PAH2 100.00 105 100.00 100.00 2.50e-69 BMRB 6899 PAH2 100.00 105 100.00 100.00 2.50e-69 PDB 1E91 "Structure Of The Complex Of The Mad1-Sin3b Interaction Domains" 80.95 85 100.00 100.00 3.07e-54 PDB 1PD7 "Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b" 80.95 85 100.00 100.00 3.07e-54 PDB 2F05 "Solution Structure Of Free Pah2 Domain Of Msin3b" 100.00 105 99.05 99.05 9.79e-69 GB AAH51536 "Sin3b protein, partial [Mus musculus]" 100.00 190 99.05 99.05 3.20e-68 GB EDL10815 "transcriptional regulator, SIN3B (yeast), isoform CRA_c [Mus musculus]" 100.00 893 99.05 99.05 2.94e-63 GB EDL90863 "rCG38713, isoform CRA_e [Rattus norvegicus]" 100.00 231 98.10 98.10 1.55e-66 GB EDL90864 "rCG38713, isoform CRA_f [Rattus norvegicus]" 100.00 841 98.10 98.10 1.31e-62 REF XP_006751561 "PREDICTED: paired amphipathic helix protein Sin3b-like [Leptonychotes weddellii]" 82.86 342 98.85 98.85 3.37e-52 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $mSin3B-PAH2 Mouse 10090 Eukaryota Metazoa Mus musculus SIN3B stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $mSin3B-PAH2 'recombinant technology' 'E. coli' Escherichia coli pBL21 plasmid pGEX2T stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Typical_sample _Saveframe_category sample _Sample_type solution _Details ; Trace amounts of Sodium azide and protease inhibitors were added for conservation ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mSin3B-PAH2 1.0 mM '[U-100% 13C; U-100% 15N]' 'Potassium Phosphate' 50 mM . 'Potassium Chloride' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task 'Data processing' stop_ _Details . _Citation_label $citation_1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.9 loop_ _Task 'Spectral analysis' stop_ _Details . _Citation_label $citation_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $Typical_sample save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $Typical_sample save_ save_CBCA(CO)NNH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NNH _Sample_label $Typical_sample save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $Typical_sample save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 na temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Typical_sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name PAH2 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLU CA C 57.582 0.200 1 2 . 1 GLU CB C 30.111 0.300 1 3 . 1 GLU C C 177.008 0.100 1 4 . 1 GLU H H 8.902 0.030 1 5 . 1 GLU N N 123.045 0.200 1 6 . 2 SER CA C 58.802 0.200 1 7 . 2 SER CB C 64.062 0.300 1 8 . 2 SER C C 174.483 0.100 1 9 . 2 SER H H 8.277 0.030 1 10 . 2 SER N N 115.643 0.200 1 11 . 3 ASP CA C 54.787 0.200 1 12 . 3 ASP CB C 41.618 0.300 1 13 . 3 ASP C C 176.495 0.100 1 14 . 3 ASP H H 8.210 0.030 1 15 . 3 ASP N N 122.305 0.200 1 16 . 4 SER CA C 58.511 0.200 1 17 . 4 SER CB C 64.403 0.300 1 18 . 4 SER C C 175.144 0.100 1 19 . 4 SER H H 8.214 0.030 1 20 . 4 SER N N 115.766 0.200 1 21 . 5 VAL CA C 63.972 0.200 1 22 . 5 VAL CB C 32.913 0.300 1 23 . 5 VAL C C 176.880 0.100 1 24 . 5 VAL H H 8.258 0.030 1 25 . 5 VAL N N 122.922 0.200 1 26 . 6 GLU CA C 58.206 0.200 1 27 . 6 GLU CB C 30.339 0.300 1 28 . 6 GLU C C 177.479 0.100 1 29 . 6 GLU H H 8.492 0.030 1 30 . 6 GLU N N 122.181 0.200 1 31 . 7 PHE CA C 59.354 0.200 1 32 . 7 PHE CB C 39.877 0.300 1 33 . 7 PHE C C 176.066 0.100 1 34 . 7 PHE H H 8.255 0.030 1 35 . 7 PHE N N 121.071 0.200 1 36 . 8 ASN CA C 54.811 0.200 1 37 . 8 ASN CB C 39.044 0.300 1 38 . 8 ASN C C 176.773 0.100 1 39 . 8 ASN H H 8.295 0.030 1 40 . 8 ASN N N 119.221 0.200 1 41 . 9 ASN CA C 54.972 0.200 1 42 . 9 ASN CB C 38.854 0.300 1 43 . 9 ASN C C 177.008 0.100 1 44 . 9 ASN H H 8.647 0.030 1 45 . 9 ASN N N 119.961 0.200 1 46 . 10 ALA CA C 55.200 0.200 1 47 . 10 ALA CB C 18.997 0.300 1 48 . 10 ALA C C 178.972 0.100 1 49 . 10 ALA H H 8.354 0.030 1 50 . 10 ALA N N 124.772 0.200 1 51 . 11 ILE CA C 63.110 0.200 1 52 . 11 ILE CB C 38.086 0.300 1 53 . 11 ILE C C 178.283 0.100 1 54 . 11 ILE H H 8.100 0.030 1 55 . 11 ILE N N 118.234 0.200 1 56 . 12 SER CA C 61.516 0.200 1 57 . 12 SER C C 176.923 0.100 1 58 . 12 SER H H 8.186 0.030 1 59 . 12 SER N N 116.753 0.200 1 60 . 13 TYR CA C 61.641 0.200 1 61 . 13 TYR CB C 41.919 0.300 1 62 . 13 TYR C C 176.976 0.100 1 63 . 13 TYR H H 8.092 0.030 1 64 . 13 TYR N N 123.785 0.200 1 65 . 14 VAL CA C 67.305 0.200 1 66 . 14 VAL CB C 30.169 0.300 1 67 . 14 VAL C C 178.018 0.100 1 68 . 14 VAL H H 8.279 0.030 1 69 . 14 VAL N N 115.520 0.200 1 70 . 15 ASN CA C 56.075 0.200 1 71 . 15 ASN CB C 38.614 0.300 1 72 . 15 ASN C C 177.718 0.100 1 73 . 15 ASN H H 8.197 0.030 1 74 . 15 ASN N N 117.370 0.200 1 75 . 16 LYS CA C 59.873 0.200 1 76 . 16 LYS CB C 32.582 0.300 1 77 . 16 LYS C C 178.831 0.100 1 78 . 16 LYS H H 8.010 0.030 1 79 . 16 LYS N N 123.785 0.200 1 80 . 17 ILE CA C 64.105 0.200 1 81 . 17 ILE CB C 37.062 0.300 1 82 . 17 ILE C C 177.259 0.100 1 83 . 17 ILE H H 7.625 0.030 1 84 . 17 ILE N N 120.207 0.200 1 85 . 18 LYS CA C 59.856 0.200 1 86 . 18 LYS CB C 32.931 0.300 1 87 . 18 LYS C C 179.449 0.100 1 88 . 18 LYS H H 8.058 0.030 1 89 . 18 LYS N N 119.714 0.200 1 90 . 19 THR CA C 65.747 0.200 1 91 . 19 THR CB C 69.508 0.300 1 92 . 19 THR C C 176.587 0.100 1 93 . 19 THR H H 7.893 0.030 1 94 . 19 THR N N 111.325 0.200 1 95 . 20 ARG CA C 56.416 0.200 1 96 . 20 ARG CB C 28.350 0.300 1 97 . 20 ARG C C 177.276 0.100 1 98 . 20 ARG H H 8.090 0.030 1 99 . 20 ARG N N 123.415 0.200 1 100 . 21 PHE CA C 57.195 0.200 1 101 . 21 PHE CB C 38.039 0.300 1 102 . 21 PHE C C 177.753 0.100 1 103 . 21 PHE H H 7.348 0.030 1 104 . 21 PHE N N 113.669 0.200 1 105 . 22 LEU CA C 58.969 0.200 1 106 . 22 LEU CB C 42.770 0.300 1 107 . 22 LEU C C 178.230 0.100 1 108 . 22 LEU H H 7.243 0.030 1 109 . 22 LEU N N 126.006 0.200 1 110 . 23 ASP CA C 54.235 0.200 1 111 . 23 ASP CB C 40.742 0.300 1 112 . 23 ASP C C 175.651 0.100 1 113 . 23 ASP H H 8.666 0.030 1 114 . 23 ASP N N 113.176 0.200 1 115 . 24 HIS CA C 54.073 0.200 1 116 . 24 HIS CB C 31.054 0.300 1 117 . 24 HIS H H 7.761 0.030 1 118 . 24 HIS N N 117.247 0.200 1 119 . 25 PRO CA C 65.276 0.200 1 120 . 25 PRO C C 177.559 0.100 1 121 . 26 GLU CA C 59.405 0.200 1 122 . 26 GLU CB C 27.531 0.300 1 123 . 26 GLU C C 178.813 0.100 1 124 . 26 GLU H H 10.290 0.030 1 125 . 26 GLU N N 121.564 0.200 1 126 . 27 ILE CA C 64.474 0.200 1 127 . 27 ILE CB C 37.319 0.300 1 128 . 27 ILE C C 177.683 0.100 1 129 . 27 ILE H H 8.150 0.030 1 130 . 27 ILE N N 123.168 0.200 1 131 . 28 TYR CA C 60.991 0.200 1 132 . 28 TYR CB C 38.836 0.300 1 133 . 28 TYR C C 176.623 0.100 1 134 . 28 TYR H H 6.806 0.030 1 135 . 28 TYR N N 119.591 0.200 1 136 . 29 ARG CA C 59.936 0.200 1 137 . 29 ARG CB C 30.287 0.300 1 138 . 29 ARG C C 179.414 0.100 1 139 . 29 ARG H H 8.401 0.030 1 140 . 29 ARG N N 117.370 0.200 1 141 . 30 SER CA C 62.674 0.200 1 142 . 30 SER CB C 63.000 0.500 1 143 . 30 SER C C 175.863 0.100 1 144 . 30 SER H H 8.176 0.030 1 145 . 30 SER N N 116.507 0.200 1 146 . 31 PHE CA C 61.408 0.200 1 147 . 31 PHE CB C 38.890 0.300 1 148 . 31 PHE C C 175.810 0.100 1 149 . 31 PHE H H 8.245 0.030 1 150 . 31 PHE N N 123.415 0.200 1 151 . 32 LEU CA C 57.651 0.200 1 152 . 32 LEU CB C 42.033 0.300 1 153 . 32 LEU C C 179.325 0.100 1 154 . 32 LEU H H 7.967 0.030 1 155 . 32 LEU N N 117.740 0.200 1 156 . 33 GLU CA C 59.616 0.200 1 157 . 33 GLU CB C 29.988 0.300 1 158 . 33 GLU C C 179.661 0.100 1 159 . 33 GLU H H 7.885 0.030 1 160 . 33 GLU N N 119.097 0.200 1 161 . 34 ILE CA C 65.149 0.200 1 162 . 34 ILE CB C 38.367 0.300 1 163 . 34 ILE C C 178.089 0.100 1 164 . 34 ILE H H 7.975 0.030 1 165 . 34 ILE N N 122.305 0.200 1 166 . 35 LEU CA C 57.700 0.200 1 167 . 35 LEU CB C 41.658 0.300 1 168 . 35 LEU C C 178.902 0.100 1 169 . 35 LEU H H 7.791 0.030 1 170 . 35 LEU N N 119.467 0.200 1 171 . 36 HIS CA C 58.695 0.200 1 172 . 36 HIS CB C 29.763 0.300 1 173 . 36 HIS C C 177.736 0.100 1 174 . 36 HIS H H 8.626 0.030 1 175 . 36 HIS N N 117.740 0.200 1 176 . 37 THR CA C 66.929 0.200 1 177 . 37 THR CB C 68.873 0.300 1 178 . 37 THR C C 175.634 0.100 1 179 . 37 THR H H 8.337 0.030 1 180 . 37 THR N N 117.370 0.200 1 181 . 38 TYR CA C 61.010 0.200 1 182 . 38 TYR CB C 39.066 0.300 1 183 . 38 TYR C C 177.188 0.100 1 184 . 38 TYR H H 8.272 0.030 1 185 . 38 TYR N N 122.181 0.200 1 186 . 39 GLN CA C 58.525 0.200 1 187 . 39 GLN CB C 29.454 0.300 1 188 . 39 GLN C C 177.930 0.100 1 189 . 39 GLN H H 8.323 0.030 1 190 . 39 GLN N N 117.370 0.200 1 191 . 40 LYS CA C 58.692 0.200 1 192 . 40 LYS CB C 32.807 0.300 1 193 . 40 LYS C C 178.336 0.100 1 194 . 40 LYS H H 7.967 0.030 1 195 . 40 LYS N N 119.467 0.200 1 196 . 41 GLU CA C 57.687 0.200 1 197 . 41 GLU CB C 30.050 0.300 1 198 . 41 GLU C C 177.559 0.100 1 199 . 41 GLU H H 8.042 0.030 1 200 . 41 GLU N N 118.974 0.200 1 201 . 42 GLN CA C 56.160 0.200 1 202 . 42 GLN CB C 29.305 0.300 1 203 . 42 GLN C C 176.605 0.100 1 204 . 42 GLN H H 7.863 0.030 1 205 . 42 GLN N N 117.740 0.200 1 206 . 43 LEU CA C 55.643 0.200 1 207 . 43 LEU CB C 42.718 0.300 1 208 . 43 LEU C C 177.276 0.100 1 209 . 43 LEU H H 7.720 0.030 1 210 . 43 LEU N N 120.207 0.200 1 211 . 44 HIS CA C 55.979 0.200 1 212 . 44 HIS CB C 30.050 0.300 1 213 . 44 HIS C C 175.351 0.100 1 214 . 44 HIS H H 8.211 0.030 1 215 . 44 HIS N N 119.221 0.200 1 216 . 45 THR CA C 62.096 0.200 1 217 . 45 THR CB C 70.587 0.300 1 218 . 45 THR C C 174.715 0.100 1 219 . 45 THR H H 8.167 0.030 1 220 . 45 THR N N 115.520 0.200 1 221 . 46 LYS CA C 57.214 0.200 1 222 . 46 LYS CB C 32.882 0.300 1 223 . 46 LYS C C 177.294 0.100 1 224 . 46 LYS H H 8.405 0.030 1 225 . 46 LYS N N 123.785 0.200 1 226 . 47 GLY CA C 45.369 0.200 1 227 . 47 GLY C C 173.849 0.100 1 228 . 47 GLY H H 8.632 0.030 1 229 . 47 GLY N N 110.585 0.200 1 230 . 48 ARG CA C 53.784 0.200 1 231 . 48 ARG CB C 30.707 0.300 1 232 . 48 ARG H H 7.916 0.030 1 233 . 48 ARG N N 120.824 0.200 1 234 . 49 PRO CA C 63.330 0.200 1 235 . 49 PRO C C 176.305 0.100 1 236 . 50 PHE CA C 57.604 0.200 1 237 . 50 PHE CB C 40.281 0.300 1 238 . 50 PHE C C 175.210 0.100 1 239 . 50 PHE H H 8.260 0.030 1 240 . 50 PHE N N 120.701 0.200 1 241 . 51 ARG CA C 55.844 0.200 1 242 . 51 ARG CB C 31.301 0.300 1 243 . 51 ARG C C 175.952 0.100 1 244 . 51 ARG H H 8.321 0.030 1 245 . 51 ARG N N 124.032 0.200 1 246 . 52 GLY CA C 44.940 0.200 1 247 . 52 GLY C C 173.408 0.100 1 248 . 52 GLY H H 7.797 0.030 1 249 . 52 GLY N N 109.845 0.200 1 250 . 53 MET CA C 56.355 0.200 1 251 . 53 MET C C 175.899 0.100 1 252 . 53 MET H H 8.796 0.030 1 253 . 53 MET N N 121.549 0.200 1 254 . 54 SER CA C 57.514 0.200 1 255 . 54 SER CB C 66.184 0.300 1 256 . 54 SER C C 175.139 0.100 1 257 . 54 SER H H 8.945 0.030 1 258 . 54 SER N N 120.454 0.200 1 259 . 55 GLU CA C 60.693 0.200 1 260 . 55 GLU CB C 29.891 0.300 1 261 . 55 GLU C C 178.266 0.100 1 262 . 55 GLU H H 9.017 0.030 1 263 . 55 GLU N N 121.318 0.200 1 264 . 56 GLU CA C 60.058 0.200 1 265 . 56 GLU CB C 29.742 0.300 1 266 . 56 GLU C C 173.885 0.100 1 267 . 56 GLU H H 8.689 0.030 1 268 . 56 GLU N N 118.480 0.200 1 269 . 57 GLU CA C 59.486 0.200 1 270 . 57 GLU CB C 30.633 0.300 1 271 . 57 GLU C C 179.096 0.100 1 272 . 57 GLU H H 7.921 0.030 1 273 . 57 GLU N N 120.948 0.200 1 274 . 58 VAL CA C 66.480 0.200 1 275 . 58 VAL CB C 31.360 0.300 1 276 . 58 VAL C C 177.206 0.100 1 277 . 58 VAL H H 8.135 0.030 1 278 . 58 VAL N N 120.454 0.200 1 279 . 59 PHE CA C 62.319 0.200 1 280 . 59 PHE CB C 39.049 0.300 1 281 . 59 PHE C C 177.789 0.100 1 282 . 59 PHE H H 8.256 0.030 1 283 . 59 PHE N N 119.467 0.200 1 284 . 60 THR CA C 66.932 0.200 1 285 . 60 THR CB C 69.284 0.300 1 286 . 60 THR C C 176.234 0.100 1 287 . 60 THR H H 8.216 0.030 1 288 . 60 THR N N 115.766 0.200 1 289 . 61 GLU CA C 59.265 0.200 1 290 . 61 GLU CB C 29.808 0.300 1 291 . 61 GLU C C 180.067 0.100 1 292 . 61 GLU H H 7.975 0.030 1 293 . 61 GLU N N 120.578 0.200 1 294 . 62 VAL CA C 66.678 0.200 1 295 . 62 VAL CB C 40.305 0.300 1 296 . 62 VAL C C 176.587 0.100 1 297 . 62 VAL H H 8.275 0.030 1 298 . 62 VAL N N 120.824 0.200 1 299 . 63 ALA CA C 55.231 0.200 1 300 . 63 ALA CB C 18.128 0.300 1 301 . 63 ALA C C 180.067 0.100 1 302 . 63 ALA H H 8.451 0.030 1 303 . 63 ALA N N 122.181 0.200 1 304 . 64 ASN CA C 55.540 0.200 1 305 . 64 ASN CB C 39.049 0.300 1 306 . 64 ASN C C 177.700 0.100 1 307 . 64 ASN H H 7.451 0.030 1 308 . 64 ASN N N 114.286 0.200 1 309 . 65 LEU CA C 57.222 0.200 1 310 . 65 LEU CB C 42.893 0.300 1 311 . 65 LEU C C 178.425 0.100 1 312 . 65 LEU H H 7.631 0.030 1 313 . 65 LEU N N 121.194 0.200 1 314 . 66 PHE CA C 53.165 0.200 1 315 . 66 PHE CB C 37.201 0.300 1 316 . 66 PHE C C 174.821 0.100 1 317 . 66 PHE H H 8.131 0.030 1 318 . 66 PHE N N 114.903 0.200 1 319 . 67 ARG CA C 58.625 0.200 1 320 . 67 ARG CB C 30.104 0.300 1 321 . 67 ARG C C 177.789 0.100 1 322 . 67 ARG H H 7.014 0.030 1 323 . 67 ARG N N 120.824 0.200 1 324 . 68 GLY CA C 45.648 0.200 1 325 . 68 GLY C C 174.326 0.100 1 326 . 68 GLY H H 9.345 0.030 1 327 . 68 GLY N N 115.150 0.200 1 328 . 69 GLN CA C 52.496 0.200 1 329 . 69 GLN CB C 26.930 0.300 1 330 . 69 GLN C C 176.164 0.100 1 331 . 69 GLN H H 8.484 0.030 1 332 . 69 GLN N N 120.454 0.200 1 333 . 70 GLU CA C 60.872 0.200 1 334 . 70 GLU CB C 29.507 0.300 1 335 . 70 GLU C C 178.478 0.100 1 336 . 70 GLU H H 8.605 0.030 1 337 . 70 GLU N N 120.578 0.200 1 338 . 71 ASP CA C 56.462 0.200 1 339 . 71 ASP CB C 38.932 0.300 1 340 . 71 ASP C C 178.372 0.100 1 341 . 71 ASP H H 8.972 0.030 1 342 . 71 ASP N N 119.221 0.200 1 343 . 72 LEU CA C 56.795 0.200 1 344 . 72 LEU CB C 42.024 0.300 1 345 . 72 LEU C C 180.421 0.100 1 346 . 72 LEU H H 7.761 0.030 1 347 . 72 LEU N N 119.591 0.200 1 348 . 73 LEU CA C 57.706 0.200 1 349 . 73 LEU CB C 42.024 0.300 1 350 . 73 LEU C C 175.916 0.100 1 351 . 73 LEU H H 8.025 0.030 1 352 . 73 LEU N N 119.961 0.200 1 353 . 74 SER CA C 61.717 0.200 1 354 . 74 SER CB C 63.152 0.300 1 355 . 74 SER C C 177.064 0.100 1 356 . 74 SER H H 8.018 0.030 1 357 . 74 SER N N 113.422 0.200 1 358 . 75 GLU CA C 57.486 0.200 1 359 . 75 GLU CB C 30.611 0.300 1 360 . 75 GLU C C 177.577 0.100 1 361 . 75 GLU H H 7.887 0.030 1 362 . 75 GLU N N 119.097 0.200 1 363 . 76 PHE CA C 62.203 0.200 1 364 . 76 PHE C C 176.711 0.100 1 365 . 76 PHE H H 7.839 0.030 1 366 . 76 PHE N N 121.441 0.200 1 367 . 77 GLY CA C 46.941 0.200 1 368 . 77 GLY C C 175.510 0.100 1 369 . 77 GLY H H 8.415 0.030 1 370 . 77 GLY N N 103.800 0.200 1 371 . 78 GLN CA C 57.012 0.200 1 372 . 78 GLN CB C 29.430 0.300 1 373 . 78 GLN C C 176.782 0.100 1 374 . 78 GLN H H 7.407 0.030 1 375 . 78 GLN N N 117.493 0.200 1 376 . 79 PHE CA C 58.789 0.200 1 377 . 79 PHE CB C 43.657 0.300 1 378 . 79 PHE C C 178.902 0.100 1 379 . 79 PHE H H 7.501 0.030 1 380 . 79 PHE N N 120.453 0.200 1 381 . 80 LEU CA C 57.616 0.200 1 382 . 80 LEU H H 8.676 0.030 1 383 . 80 LEU N N 117.740 0.200 1 384 . 81 PRO CA C 62.834 0.200 1 385 . 81 PRO C C 175.704 0.100 1 386 . 82 GLU CA C 57.931 0.200 1 387 . 82 GLU C C 178.407 0.100 1 388 . 82 GLU H H 8.566 0.030 1 389 . 82 GLU N N 122.922 0.200 1 390 . 83 ALA CA C 54.252 0.200 1 391 . 83 ALA CB C 18.198 0.300 1 392 . 83 ALA C C 178.849 0.100 1 393 . 83 ALA H H 8.138 0.030 1 394 . 83 ALA N N 122.798 0.200 1 395 . 84 LYS CA C 58.298 0.200 1 396 . 84 LYS CB C 39.364 0.300 1 397 . 84 LYS C C 175.916 0.100 1 398 . 84 LYS H H 7.960 0.030 1 399 . 84 LYS N N 116.136 0.200 1 400 . 85 ARG CA C 57.866 0.200 1 401 . 85 ARG CB C 31.382 0.300 1 402 . 85 ARG C C 177.400 0.100 1 403 . 85 ARG H H 7.567 0.030 1 404 . 85 ARG N N 119.756 0.200 1 405 . 86 SER CA C 59.589 0.200 1 406 . 86 SER CB C 64.777 0.300 1 407 . 86 SER C C 174.538 0.100 1 408 . 86 SER H H 8.066 0.030 1 409 . 86 SER N N 113.546 0.200 1 410 . 87 LEU CA C 55.688 0.200 1 411 . 87 LEU CB C 42.923 0.300 1 412 . 87 LEU C C 178.919 0.100 1 413 . 87 LEU H H 8.028 0.030 1 414 . 87 LEU N N 121.935 0.200 1 415 . 88 PHE CA C 57.414 0.200 1 416 . 88 PHE CB C 39.362 0.300 1 417 . 88 PHE C C 176.058 0.100 1 418 . 88 PHE H H 8.097 0.030 1 419 . 88 PHE N N 117.987 0.200 1 420 . 89 THR CA C 61.830 0.200 1 421 . 89 THR CB C 70.330 0.300 1 422 . 89 THR C C 175.280 0.100 1 423 . 89 THR H H 7.958 0.030 1 424 . 89 THR N N 112.682 0.200 1 425 . 90 GLY CA C 45.603 0.200 1 426 . 90 GLY C C 174.114 0.100 1 427 . 90 GLY H H 8.117 0.030 1 428 . 90 GLY N N 110.338 0.200 1 429 . 91 ASN CA C 53.382 0.200 1 430 . 91 ASN CB C 39.508 0.300 1 431 . 91 ASN C C 175.987 0.100 1 432 . 91 ASN H H 8.443 0.030 1 433 . 91 ASN N N 118.850 0.200 1 434 . 92 GLY CA C 45.681 0.200 1 435 . 92 GLY C C 174.432 0.100 1 436 . 92 GLY H H 8.527 0.030 1 437 . 92 GLY N N 109.598 0.200 1 438 . 93 SER CA C 58.497 0.200 1 439 . 93 SER CB C 64.414 0.300 1 440 . 93 SER C C 174.768 0.100 1 441 . 93 SER H H 8.200 0.030 1 442 . 93 SER N N 115.643 0.200 1 443 . 94 ALA CA C 53.097 0.200 1 444 . 94 ALA CB C 19.642 0.300 1 445 . 94 ALA C C 177.965 0.100 1 446 . 94 ALA H H 8.443 0.030 1 447 . 94 ALA N N 125.759 0.200 1 448 . 95 GLU CA C 56.911 0.200 1 449 . 95 GLU CB C 30.670 0.300 1 450 . 95 GLU C C 176.852 0.100 1 451 . 95 GLU H H 8.361 0.030 1 452 . 95 GLU N N 119.344 0.200 1 453 . 96 MET CA C 55.807 0.200 1 454 . 96 MET CB C 33.592 0.300 1 455 . 96 MET C C 176.234 0.100 1 456 . 96 MET H H 8.306 0.030 1 457 . 96 MET N N 120.701 0.200 1 458 . 97 ASN CA C 53.399 0.200 1 459 . 97 ASN CB C 39.362 0.300 1 460 . 97 ASN C C 175.369 0.100 1 461 . 97 ASN H H 8.457 0.030 1 462 . 97 ASN N N 119.714 0.200 1 463 . 98 SER CA C 58.871 0.200 1 464 . 98 SER CB C 64.127 0.300 1 465 . 98 SER C C 175.245 0.100 1 466 . 98 SER H H 8.369 0.030 1 467 . 98 SER N N 116.383 0.200 1 468 . 99 GLY CA C 45.452 0.200 1 469 . 99 GLY C C 174.273 0.100 1 470 . 99 GLY H H 8.497 0.030 1 471 . 99 GLY N N 110.708 0.200 1 472 . 100 GLN CA C 55.845 0.200 1 473 . 100 GLN CB C 30.011 0.300 1 474 . 100 GLN C C 176.005 0.100 1 475 . 100 GLN H H 8.193 0.030 1 476 . 100 GLN N N 119.961 0.200 1 477 . 101 LYS CA C 56.361 0.200 1 478 . 101 LYS CB C 33.648 0.300 1 479 . 101 LYS C C 176.252 0.100 1 480 . 101 LYS H H 8.449 0.030 1 481 . 101 LYS N N 122.798 0.200 1 482 . 102 ASN CA C 53.442 0.200 1 483 . 102 ASN CB C 39.467 0.300 1 484 . 102 ASN C C 175.157 0.100 1 485 . 102 ASN H H 8.565 0.030 1 486 . 102 ASN N N 120.578 0.200 1 487 . 103 GLU CA C 56.510 0.200 1 488 . 103 GLU CB C 30.957 0.300 1 489 . 103 GLU C C 176.234 0.100 1 490 . 103 GLU H H 8.478 0.030 1 491 . 103 GLU N N 121.441 0.200 1 492 . 104 GLU CA C 56.594 0.200 1 493 . 104 GLU CB C 30.738 0.300 1 494 . 104 GLU C C 175.492 0.100 1 495 . 104 GLU H H 8.419 0.030 1 496 . 104 GLU N N 122.675 0.200 1 497 . 105 LYS CA C 57.581 0.200 1 498 . 105 LYS CB C 34.230 0.300 1 499 . 105 LYS H H 7.969 0.030 1 500 . 105 LYS N N 127.733 0.200 1 stop_ save_